Biochemistry articles within Nature

Featured

  • Article
    | Open Access

    A structure of the MRAS–SHOC2–PP1C complex supports a RAS-driven and multi-molecular model for RAF activation in which individual RAS–GTP molecules recruit RAF–14-3-3 and SHOC2–PP1C to activate the downstream pathway.

    • Zachary J. Hauseman
    • , Michelle Fodor
    •  & Daniel A. King
  • Article
    | Open Access

    The Polα–primase-associated CST complex organizes telomeric C-strand DNA synthesis, and, in combination with telomerase, it carries out complete replication of the single-stranded DNA overhang found at human telomeres.

    • Arthur J. Zaug
    • , Karen J. Goodrich
    •  & Thomas R. Cech
  • Article
    | Open Access

    The biosynthetic pathway of strychnine, brucine and diaboline is described, and the biosynthesis of these complex, pharmacologically active compounds has been successfully recapitulated in Nicotiana benthamiana from an upstream intermediate.

    • Benke Hong
    • , Dagny Grzech
    •  & Sarah E. O’Connor
  • Article
    | Open Access

    The evolutionarily conserved RNA-binding protein GTSF1 and its homologues interact with members of the PIWI class of Argonaute proteins, increasing the efficiency of the RNA-cleaving activity of PIWI proteins, an essential function across the animal kingdom.

    • Amena Arif
    • , Shannon Bailey
    •  & Phillip D. Zamore
  • Article
    | Open Access

    Cryo-electron microscopy structure, molecular dynamics and biochemical analyses of the SHOC2–PP1C–MRAS complex demonstrate the dependence of the complex formation on RAS–GTP and identify the determinants of RAS isoform preference for SHOC2–PP1C and specificity of the complex for RAF dephosphorylation.

    • Nicholas P. D. Liau
    • , Matthew C. Johnson
    •  & Jawahar Sudhamsu
  • Article
    | Open Access

    Structures of the Dcr-2–Loqs-PD complex while it is processing a double-stranded RNA (dsRNA) substrate elucidate the interactions between Dcr-2 and Loqs-PD, and show that Dcr-2 undergoes substantial conformational changes during a dsRNA-processing cycle.

    • Shichen Su
    • , Jia Wang
    •  & Jinbiao Ma
  • Article
    | Open Access

    Cryo-electron microscopy structures of Drosophila Dicer-2–R2D2 complexes with and without small interfering RNA reveal how the RNA is presented to Argonaute in the correct orientation for viral gene silencing.

    • Sonomi Yamaguchi
    • , Masahiro Naganuma
    •  & Osamu Nureki
  • Article |

    Single-molecule spectroscopy and structural studies were used to examine the dynamics of association of eIF1A and eIF5B with the human translation initiation complex and their role in presenting tRNA to the complex to initiate translation.

    • Christopher P. Lapointe
    • , Rosslyn Grosely
    •  & Joseph D. Puglisi
  • Article
    | Open Access

    Cryo-electron microscopy structures of the sequential assembly of the CMG replicative helicase on a chromatinized origin of replication provide insights into the mechanism through which DNA melting is initiated by ATP binding.

    • Jacob S. Lewis
    • , Marta H. Gross
    •  & Alessandro Costa
  • Research Briefing |

    The organizational principles of the eukaryotic cell cycle have yet to be pinned down, and two opposing models have been put forward. Genetic and proteomics analyses in a model eukaryote, fission yeast, reveal that the cell cycle is organized through a hybrid of both models, although the contribution of one strongly outweighs the other.

  • Article
    | Open Access

    The core cell cycle is largely driven by increasing total CDK activity together with minor differences in the substrate specificity of the CDKs initiating DNA replication and mitosis.

    • Souradeep Basu
    • , Jessica Greenwood
    •  & Paul Nurse
  • Article |

    Structural determination of GAT1 using cryo-electron microscopy provides insights into the biology and pharmacology of this GABA transporter.

    • Zenia Motiwala
    • , Nanda Gowtham Aduri
    •  & Cornelius Gati
  • Article
    | Open Access

    Chimeric triterpene synthases are identified that catalyse non-squalene-dependent triterpene biosynthesis.

    • Hui Tao
    • , Lukas Lauterbach
    •  & Tiangang Liu
  • News & Views |

    The seas are acidifying as a result of carbon dioxide emissions. It now emerges that this will alter the solubility of the shells of marine organisms called diatoms — and thereby change the distribution of nutrients and plankton in the ocean.

    • David A. Hutchins
  • Article
    | Open Access

    The development of confined organocatalysts for the enantioselective cyanosilylation of small, unbiased substrates, including 2-butanone, is shown to lead to catalysts that are as selective as enzymes, with excellent levels of control.

    • Hui Zhou
    • , Yu Zhou
    •  & Benjamin List
  • Article |

    The molecular determinants for primer synthesis are identified within the catalytic domain of primase-polymerase enzymes, elucidating the mechanisms underlying initiation of primer synthesis.

    • Arthur W. H. Li
    • , Katerina Zabrady
    •  & Aidan J. Doherty
  • Article |

    Herpesvirus microRNAs interfere directly with host cell microRNA processing, thereby disrupting mitochondrial architecture, evading intrinsic host defences and driving the switch from latent to lytic infection.

    • Thomas Hennig
    • , Archana B. Prusty
    •  & Bhupesh K. Prusty
  • Article |

    Cryo-electron microscopy structures of GPR56 and latrophilin 3 show how the released tethered agonist peptide interacts with the transmembrane domain, suggesting a model for the activation mechanism of adhesion G-protein-coupled receptors.

    • Ximena Barros-Álvarez
    • , Robert M. Nwokonko
    •  & Georgios Skiniotis
  • Article
    | Open Access

    A study using a biochemical screen of 57 phages in two bacterial species identifies and characterizes proteins enabling phages to evade CBASS and Pycsar immune systems, and describes the mechanisms involved.

    • Samuel J. Hobbs
    • , Tanita Wein
    •  & Philip J. Kranzusch
  • Article |

    Cryo-electron microscopy structures of the bacterial O-antigen ligase WaaL, combined with genetics, biochemistry and molecular dynamics simulations, provide insight into the mechanism by which WaaL catalyses the biosynthesis of lipopolysaccharide.

    • Khuram U. Ashraf
    • , Rie Nygaard
    •  & Filippo Mancia
  • Article |

    A biocatalytic enzyme originating from bacteria, EneIRED, facilitates amine-activated conjugate alkene reduction followed by reductive amination, efficiently preparing chiral amine diastereomers, which are commonly used in pharmaceuticals and agrochemicals. 

    • Thomas W. Thorpe
    • , James R. Marshall
    •  & Nicholas J. Turner
  • Article |

    A cryo-electron microscopy analysis reveals how HAS selects its substrates, hydrolyses the first substrate to prime the synthesis reaction, opens a hyaluronan-conducting transmembrane channel, ensures alternating substrate polymerization and coordinates hyaluronan inside its transmembrane pore.

    • Finn P. Maloney
    • , Jeremi Kuklewicz
    •  & Jochen Zimmer
  • Article
    | Open Access

    Cryo-electron microscopy structures of ligand-free, agonist-bound and antagonist-bound Ste2 show that this class D1 G protein-coupled receptor has a distinct mechanism of activation compared with other receptor classes.

    • Vaithish Velazhahan
    • , Ning Ma
    •  & Christopher G. Tate
  • News & Views |

    It is textbook knowledge that some bacteria can generate methane enzymatically. A study now provides evidence that an alternative, non-enzymatic mode of methane production could occur in all metabolically active cells.

    • Chang Liu
    •  & Jingyao Zhang
  • Article |

    A bacterial enzyme is characterized and demonstrated to have Ni2+-dependent activity and high specificity for free guanidine enabling the bacteria to use guanidine as the sole nitrogen source for growth.

    • D. Funck
    • , M. Sinn
    •  & J. S. Hartig
  • Article |

    Combining NMR spectroscopy-derived pseudocontact shifts (PCSs) with Carr–Purcell–Meiboom–Gill (CPMG) relaxation dispersion enables protein structure determination of lowly populated high-energy states that are essential for macromolecular function.

    • John B. Stiller
    • , Renee Otten
    •  & Dorothee Kern
  • Research Briefing |

    Proteins adopt unstable, high-energy states that exist for fractions of a second but can have key biological roles. A new method of determining high-resolution structures of such states using a form of nuclear magnetic resonance reveals how small changes in protein shape are essential to their function.

  • Article |

    A study presents a biocatalytic method for the formation of sterically hindered biaryl bonds, providing a tunable approach for assembling molecules with catalyst-controlled reactivity, site selectivity and atroposelectivity.

    • Lara E. Zetzsche
    • , Jessica A. Yazarians
    •  & Alison R. H. Narayan
  • Article
    | Open Access

    Cryo-electron microscopy structures of Cas9 during mismatch cleavage provide insight into the mechanisms that control off-target effects of Cas9, which will aid in the future design of high-fidelity Cas9 variants with reduced off-target cleavage.

    • Jack P. K. Bravo
    • , Mu-Sen Liu
    •  & David W. Taylor